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Cortés, J.C. et al.

Joel Cerna Cortés, Eliud Alfredo Garcia Montalvo, Jesús Muñiz, Dominique Mornet, Efrain Garrido, Federico Centeno, Bulmaro Cisneros,

Dp71f modulates GSK3-beta recruitment to the beta1-integrin adhesion complex.

Previously, it was shown that Dp71f binds to the beta1-integrin adhesion complex to modulate PC12 cell adhesion. The absence of Dp71f led to a failure in the beta1-integrin adhesion complex formation. One of the structural proteins which links the beta1-integrin cytoplasmic domain to the actin cytoskeleton is ILK. GSK3-beta is an ILK substrate and the carboxi-terminal region of dystrophin 427 is a substrate for hierarchical phosphorylation by GSK3-beta. Dp71f contains the carboxi-terminal domain present in dystrophin 427. By using co-immunoprecipitation assays, in the present work it is demonstrated that in the neuronal PC12 cell line an interaction between Dp71f and GSK3-beta occurs. This interaction was corroborated by in vitro pulldown assays. We show that GSK3-beta is recruited to the beta1-integrin complex and that a reduced expression of Dp71f induces a reduced GSK3-beta recruitment to the beta1-integrin complex. In addition, the present work establishes that adhesion of PC12 cells to laminin does not influence the phosphorylation status of Dp71f.[1]

References

Dp71f modulates GSK3-beta recruitment to the beta1-integrin adhesion complex. Cortés, J.C., Montalvo, E.A., Muñiz, J., Mornet, D., Garrido, E., Centeno, F., Cisneros, B. Neurochem. Res. (2009) [Pubmed]

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